Carboxy-lyases explained

Carboxy-lyases, also known as decarboxylases, are carbon–carbon lyases that add or remove a carboxyl group from organic compounds. These enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids.[1]

Classification and nomenclature

Carboxy-lyases are categorized under EC number 4.1.1.[2] Usually, they are named after the substrate whose decarboxylation they catalyze, for example pyruvate decarboxylase catalyzes the decarboxylation of pyruvate.

Examples

See also

Notes and References

  1. 10.1016/S0167-4838(98)00076-4. Application of α-keto acid decarboxylases in biotransformations. 1998. Iding . H.. Siegert. P.. Mesch. K.. Pohl. M.. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385. 2. 307–322. 9655924.
  2. Web site: E.C.4.1.1.- Carboxy-lyases.. www.biochem.ucl.ac.uk. 2006-11-08. https://web.archive.org/web/20061013132003/http://www.biochem.ucl.ac.uk/bsm/enzymes/ec4/ec01/ec01/index.html#. 2006-10-13. dead.
  3. 10.1126/science.aah5237. A synthetic pathway for the fixation of carbon dioxide in vitro. 2016. Schwander. Thomas. Schada von Borzyskowski. Lennart. Burgener. Simon. Cortina. Niña Socorro. Erb. Tobias J.. Science. 354. 6314. 900–904. 27856910. 5892708. 2016Sci...354..900S.